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Han, Y.* ; Yu, G.* ; Sarioglu, H. ; Caballero-Martinez, A.* ; Schlott, F.* ; Ueffing, M. ; Haase, H.* ; Peschel, C.* ; Krackhardt, A.M.

Proteomic investigation of the interactome of FMNL1 in hematopoietic cells unveils a role in calcium-dependent membrane plasticity.

J. Proteomics 78, 72-82 (2013)
Postprint Manuscript DOI PMC
Open Access Green
Formin-like 1 (FMNL1) is a formin-related protein highly expressed in hematopoietic cells and overexpressed in leukemias as well as diverse transformed cell lines. It has been described to play a role in diverse functions of hematopoietic cells such as phagocytosis of macrophages as well as polarization and cytotoxicity of T cells. However, the specific role of FMNL1 in these processes has not been clarified yet and regulation by interaction partners in primary hematopoietic cells has never been investigated. We performed a proteomic screen for investigation of the interactome of FMNL1 in primary hematopoietic cells resulting in the identification of a number of interaction partners. Bioinformatic analysis considering semantic similarity suggested the giant protein AHNAK1 to be an essential interaction partner of FMNL1. We confirmed AHNAK1 as a general binding partner for FMNL1 in diverse hematopoietic cells and demonstrate that the N-terminal part of FMNL1 binds to the C-terminus of AHNAK1. Moreover, we show that the constitutively activated form of FMNL1 (FMNL1γ) induces localization of AHNAK1 to the cell membrane. Finally, we provide evidence that overexpression or knock down of FMNL1 has an impact on the capacitative calcium influx after ionomycin-mediated activation of diverse cell lines and primary cells.
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Publication type Article: Journal article
Document type Scientific Article
Keywords FMNL1; AHNAK1; Membrane plasticity; Chronic Lymphocytic-leukemia ; Protein Interaction Network ; Beta-adrenergic Regulation ; Semantic Similarity ; Desmoyokin/ahnak Protein ; Endoplasmic-reticulum ; Regulated Exocytosis ; Complex Provides ; Ca2+ Channels ; R Package
Language
Publication Year 2013
Prepublished in Year 2012
HGF-reported in Year 2012
ISSN (print) / ISBN 1874-3919
e-ISSN 1876-7737
Journal Journal of Proteomics
Quellenangaben Volume: 78, Issue: , Pages: 72-82 Article Number: , Supplement: ,
Publisher Elsevier
Reviewing status Peer reviewed
Institute(s) CF Metabolomics & Proteomics (CF-MPC)
Institute of Molecular Immunology (IMI)
POF-Topic(s) 30203 - Molecular Targets and Therapies
30504 - Mechanisms of Genetic and Environmental Influences on Health and Disease
Research field(s) Enabling and Novel Technologies
Immune Response and Infection
PSP Element(s) G-505700-001
G-501790-002
DOI 10.1016/j.jprot.2012.11.015
WOS ID WOS:000316706800006
Scopus ID 84871780393
PubMed ID 23182705
Erfassungsdatum 2012-12-31
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